Assembly of heterobimetallic NiII–LnIII (LnIII = DyIII, TbIII, GdIII, HoIII, ErIII, YIII) complexes using a ferrocene ligand: slow relaxation of the magnetization in DyIII, TbIII and HoIII analogues

2014 ◽  
Vol 43 (23) ◽  
pp. 8921-8932 ◽  
Author(s):  
Amit Chakraborty ◽  
Prasenjit Bag ◽  
Eric Rivière ◽  
Talal Mallah ◽  
Vadapalli Chandrasekhar
Keyword(s):  
Slow Relaxation ◽  
Heterobimetallic Complexes ◽  
New Family

Structure and characterization of a new family of dinuclear 3d–4f heterobimetallic complexes [LNi(H2O)(μ-OAc)Ln(NO3)2]·CH3CN; {Ln = DyIII (1), TbIII (2), HoIII (3), GdIII (4), ErIII (5), YIII (6)} using a ferrocene-based compartmental ligand H2L.

scholarly journals An Intrinsic Characterization of Five Points in a CAT(0) Space

2020 ◽  
Vol 8 (1) ◽  
pp. 114-165
Author(s):  
Tetsu Toyoda
Keyword(s):  
Metric Space ◽  
Isometric Embedding ◽  
Metric Spaces ◽  
Necessary Conditions ◽  
New Approach ◽  
Intrinsic Characterization ◽  
New Family

AbstractGromov (2001) and Sturm (2003) proved that any four points in a CAT(0) space satisfy a certain family of inequalities. We call those inequalities the ⊠-inequalities, following the notation used by Gromov. In this paper, we prove that a metric space X containing at most five points admits an isometric embedding into a CAT(0) space if and only if any four points in X satisfy the ⊠-inequalities. To prove this, we introduce a new family of necessary conditions for a metric space to admit an isometric embedding into a CAT(0) space by modifying and generalizing Gromov’s cycle conditions. Furthermore, we prove that if a metric space satisfies all those necessary conditions, then it admits an isometric embedding into a CAT(0) space. This work presents a new approach to characterizing those metric spaces that admit an isometric embedding into a CAT(0) space.

scholarly journals Semi-Crystalline Hydrophobic Polyamidoamines: A New Family of Technological Materials?

Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1018
Author(s):  
Massimo Marcioni ◽  
Jenny Alongi ◽  
Elisabetta Ranucci ◽  
Mario Malinconico ◽  
Paola Laurienzo ◽  
...  
Keyword(s):  
Maximum Stress ◽  
Water Resistance ◽  
Prolonged Exposure ◽  
Water Soluble ◽  
Synthesis And Characterization ◽  
Molecular Weights ◽  
New Family ◽  
Methylene Groups ◽  
Methane Flame

The hitherto known polyamidoamines (PAAs) are not suitable as structural materials because they are usually water-soluble or swellable in water. This paper deals with the synthesis and characterization of semi-crystalline hydrophobic PAAs (H-PAAs) by combining different bis-sec-amines with bis-acrylamides obtained from C6–C12 bis-prim-amines. H-PAAs were initially obtained in a solution of benzyl alcohol, a solvent suitable for both monomers and polymers. Their number average molecular weights, M¯n, which were determined with 1H-NMR by evaluating the percentage of their terminal units, varied from 6000 to >10,000. The solubility, thermal properties, ignitability and water resistance of H-PAAs were determined. They were soluble in organic solvents, semi-crystalline and thermally stable. The most promising ones were also prepared using a bulk process, which has never been previously reported for PAA synthesis. In the form of films, these H-PAAs were apparently unaffected by water. The films underwent tensile and wettability tests. They showed similar Young moduli (260–263 MPa), whereas the maximum stress and the stress at break depended on the number of methylene groups of the starting bis-acrylamides. Their wettability was somewhat higher than that of common Nylons. Interestingly, none of the H-PAAs considered, either as films or powders, ignited after prolonged exposure to a methane flame.

Protein expression and extraction of hard-to-produce proteins in the periplasmic space of Escherichia coli v1

2021 ◽  
Author(s):  
Cristina Hernandez Rollan ◽  
Kristoffer Bach Falkenberg ◽  
Maja Rennig ◽  
Andreas Birk Bertelsen ◽  
Morten Norholm
Keyword(s):  
Protein Production ◽  
Expression System ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
E Coli ◽  
New Family ◽  
Lytic Polysaccharide Monooxygenases ◽  
Strain Bl21 ◽  
Polysaccharide Monooxygenases

E. coli is a gram-negative bacteria used mainly in academia and in some industrial scenarios, as a protein production workhorse. This is due to its ease of manipulation and the range of genetic tools available. This protocol describes how to express proteins in the periplasm E. coli with the strain BL21 (DE3) using a T7 expression system. Specifically, it describes a series of steps and tips to express "hard-to-express" proteins in E. coli, as for instance, LPMOs. The protocol is adapted from Hemsworth, G. R., Henrissat, B., Davies, G. J., and Walton, P. H. (2014) Discovery and characterization of a new family of lytic polysaccharide monooxygenases. Nat. Chem. Biol.10, 122–126. .

scholarly journals Cover Feature: Isolation and Characterization of Different Homometallic and Heterobimetallic Complexes of Nickel and Zinc Ions by Controlling  Molar Ratios and Solvents (Eur. J. Inorg. Chem. 24/2019)

2019 ◽  
Vol 2019 (24) ◽  
pp. 2862-2862
Author(s):  
Saroj Kumar Kushvaha ◽  
Selvakumar Arumugam ◽  
Bhaskaran Shankar ◽  
Rabi Shankar Sarkar ◽  
Venkatachalam Ramkumar ◽  
...  
Keyword(s):  
Zinc Ions ◽  
Molar Ratios ◽  
Heterobimetallic Complexes ◽  
Isolation And Characterization

Molecular characterization of a new family with α-Thalassemia-1 (——MA mutation)

1995 ◽  
Vol 49 (4) ◽  
pp. 294-298 ◽  
Author(s):  
Ana Villegas ◽  
Jesus Sanchez ◽  
Dolores L. Carreno ◽  
Paloma Ropero ◽  
Fernando A. Gonzalez ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
New Family

An essential Saccharomyces cerevisiae gene homologous to SNF2 encodes a helicase-related protein in a new family

1992 ◽  
Vol 12 (4) ◽  
pp. 1893-1902
Author(s):  
B C Laurent ◽  
X Yang ◽  
M Carlson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Nucleoside Triphosphate ◽  
Related Protein ◽  
New Family ◽  
Eukaryotic Proteins ◽  
Beta Galactosidase

The Saccharomyces cerevisiae SNF2 gene affects the expression of many diversely regulated genes and has been implicated in transcriptional activation. We report here the cloning and characterization of STH1, a gene that is homologous to SNF2. STH1 is essential for mitotic growth and is functionally distinct from SNF2. A bifunctional STH1-beta-galactosidase protein is located in the nucleus. The predicted 155,914-Da STH1 protein is 72% identical to SNF2 over 661 amino acids and 46% identical over another stretch of 66 amino acids. Both STH1 and SNF2 contain a putative nucleoside triphosphate-binding site and sequences resembling the consensus helicase motifs. The large region of homology shared by STH1 and SNF2 is conserved among other eukaryotic proteins, and STH1 and SNF2 appear to define a novel family of proteins related to helicases.

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